<br/>Evidence has accumulated that many non-enveloped viruses have the ability to breach membranes using a component of their capsid. This lytic component is sequestered inside the capsid during much of the virus life cycle but then becomes exposed/externalized only under specific conditions (e.g. endosomal pH). These peptides are very dynamic and appear to be highly sensitive to their environment. I will present results on the behavior of lytic peptides from the Flock House virus, which is an insect infecting model system for non-enveloped viruses. These simulation studies are aimed at characterizing the membrane binding, membrane insertion and peptide oligomerization properties of these peptides. We will further examine the influence of lipid composition and peptide concentration on the structural and energetic properties of these interactions. We have employed a multiscale approach utilizing both all-atom and coarse-grained models in these studies.

Structure and dynamics of viral lytic peptides in membrane environments

251st National Meeting (2016)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.